ID E8V213_TERSS Unreviewed; 946 AA.
AC E8V213;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN OrderedLocusNames=AciPR4_3821 {ECO:0000313|EMBL:ADV84570.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV84570.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV84570.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002467; ADV84570.1; -; Genomic_DNA.
DR RefSeq; WP_013570300.1; NC_014963.1.
DR AlphaFoldDB; E8V213; -.
DR STRING; 401053.AciPR4_3821; -.
DR KEGG; tsa:AciPR4_3821; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_0; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000006844; Chromosome.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT DOMAIN 69..609
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 739..866
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 418..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 102542 MW; D52624DA8AA58E57 CRC64;
MSTLNTFDAK ATLVSGGKNY EIYRLDSLAN KGIELARLPF SLRILLENLL RREDGVTVTA
DDITFLAKWE AKAEPSREIA YMPARVLMQD FTGVPAIVDL AAMRDAMKTL GGDPEKINPL
QPAELVIDHS VQVDEYGTAN AYDMNSLLEF QRNRERYAFL KWGQTAFRNF SAVPPGMGIC
HQVNLEYLAR VVFTTPESGD HAGQAYPDTL VGTDSHTTMV NGLGVLGWGV GGIEAEAAML
GQPVSMLVPQ VVGFKLTGKL KQGTTATDLV LTITEQLRKH GVVGKFVEFY GSGIAELPLA
DRATIANMAP EYGATCGIFP VDKETLAYLR LTGRSEAQIQ LVEDYYSAQG MFYTASSTDA
EYTSSLELDL TTVEPSIAGP KRPQDRVALS QASESFAKQL PSLYGPNANL KGDRQISRWQ
GEGGHSSQDG SIESNKAMPE PGKDGHLTTG FEPIASIKER FGFDVDEYLH HGSIVIAAIT
SCTNTSNPNV MLAAGLLAKK AVEKGLRTPP WVKTSLAPGS RVVTDYYDKA GLTQYLDALR
FQTVGYGCTT CIGNSGALPT DVSKAIDEHG LVAVSVLSGN RNFEGRINSD VRANYLMSPP
LVVAYALAGR IDFNFDTEAI GTGKDGEQVF LKDIWPSQQE VAETVANSID SSMFHKEYST
ISDGDVSWQN LKFPLGDTYG WEPDSTYIRK APYFDGMPAT PAPVTDIAGA RVLAVLGDSV
TTDHISPAGS IKLNGPAGKY LIEHGVKATD FNSYGSRRGN HEVMVRGTFA NVRLKNKLAP
GTEGGVTRLL PEDKGMSIYD ASVIYAERNV PLAILAGKEY GSGSSRDWAA KGPRLLGIRF
VLAESYERIH RSNLVGMGIL PLQFQAGDNA ESHCLTGEEI YDVPGLKEML DNKFASGKQI
TVTATDKDGE VKHIPATVRI DTPQEILYYQ HGGILQYVLR QLAGKA
//
